This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Urbonavicius, J.
Right arrow Articles by Björk, G. R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Urbonavicius, J.
Right arrow Articles by Björk, G. R.

 Previous Article  |  Next Article 

Journal of Bacteriology, October 2002, p. 5348-5357, Vol. 184, No. 19
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.19.5348-5357.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Three Modifications in the D and T Arms of tRNA Influence Translation in Escherichia coli and Expression of Virulence Genes in Shigella flexneri

Jaunius Urbonavicius, Jérôme M. B. Durand, and Glenn R. Björk*

Department of Molecular Biology, Umeå University, S-90 187 Umeå, Sweden

Received 13 March 2002/ Accepted 2 July 2002

The modified nucleosides 2'-O-methylguanosine, present at position 18 (Gm18), 5-methyluridine, present at position 54 (m5U54), and pseudouridine, present at position 55 ({Psi}55), are located in the D and T arms of tRNAs and are close in space in the three-dimensional (3D) structure of this molecule in the bacterium Escherichia coli. The formation of these modified nucleosides is catalyzed by the products of genes trmH (Gm18), trmA (m5U54), and truB ({Psi}55). The combination of trmH, trmA, and truB mutations resulting in lack of these three modifications reduced the growth rate, especially at high temperature. Moreover, the lack of three modified nucleotides in tRNA induced defects in the translation of certain codons, sensitivity to amino acid analog 3,4-dehydro-DL-proline, and an altered oxidation of some carbon compounds. The results are consistent with the suggestion that these modified nucleosides, two of which directly interact in the 3D structure of tRNA by forming a hydrogen bond between {Psi}55 and Gm18, stabilize the structure of the tRNA. Moreover, lack of {Psi}55 in tRNA of human pathogen Shigella flexneri leads to a reduced expression of several virulence-associated genes.


* Corresponding author. Mailing address: Department of Molecular Biology, Umeå University, S-90 187 Umeå, Sweden. Phone: 46-90-7856756. Fax: 46-90-772630. E-mail: glenn.bjork{at}molbiol.umu.se.


Journal of Bacteriology, October 2002, p. 5348-5357, Vol. 184, No. 19
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.19.5348-5357.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.




This article has been cited by other articles:

  • Kotelawala, L., Grayhack, E. J., Phizicky, E. M. (2008). Identification of yeast tRNA Um44 2'-O-methyltransferase (Trm44) and demonstration of a Trm44 role in sustaining levels of specific tRNASer species. RNA 14: 158-169 [Abstract] [Full Text]  
  • Watanabe, K., Nureki, O., Fukai, S., Endo, Y., Hori, H. (2006). Functional Categorization of the Conserved Basic Amino Acid Residues in TrmH (tRNA (Gm18) Methyltansferase) Enzymes. J. Biol. Chem. 281: 34630-34639 [Abstract] [Full Text]  
  • ALEXANDROV, A., GRAYHACK, E. J., PHIZICKY, E. M. (2005). tRNA m7G methyltransferase Trm8p/Trm82p: Evidence linking activity to a growth phenotype and implicating Trm82p in maintaining levels of active Trm8p. RNA 11: 821-830 [Abstract] [Full Text]  
  • Watanabe, K., Nureki, O., Fukai, S., Ishii, R., Okamoto, H., Yokoyama, S., Endo, Y., Hori, H. (2005). Roles of Conserved Amino Acid Sequence Motifs in the SpoU (TrmH) RNA Methyltransferase Family. J. Biol. Chem. 280: 10368-10377 [Abstract] [Full Text]  
  • Xing, F., Hiley, S. L., Hughes, T. R., Phizicky, E. M. (2004). The Specificities of Four Yeast Dihydrouridine Synthases for Cytoplasmic tRNAs. J. Biol. Chem. 279: 17850-17860 [Abstract] [Full Text]  
  • Ahn, K.-S., Ha, U., Jia, J., Wu, D., Jin, S. (2004). The truA gene of Pseudomonas aeruginosa is required for the expression of type III secretory genes. Microbiology 150: 539-547 [Abstract] [Full Text]  
  • Agris, P. F. (2004). Decoding the genome: a modified view. Nucleic Acids Res 32: 223-238 [Abstract] [Full Text]  
  • Pan, H., Agarwalla, S., Moustakas, D. T., Finer-Moore, J., Stroud, R. M. (2003). Structure of tRNA pseudouridine synthase TruB and its RNA complex: RNA recognition through a combination of rigid docking and induced fit. Proc. Natl. Acad. Sci. USA 100: 12648-12653 [Abstract] [Full Text]  
  • URBONAVICIUS, J., STAHL, G., DURAND, J. M.B., BEN SALEM, S. N., QIAN, Q., FARABAUGH, P. J., BJORK, G. R. (2003). Transfer RNA modifications that alter +1 frameshifting in general fail to affect -1 frameshifting. RNA 9: 760-768 [Abstract] [Full Text]